The Enzyme Database

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Accepted name: (S)-methylmalonyl-CoA decarboxylase (sodium-transporting)
Reaction: (S)-methylmalonyl-CoA + Na+[side 1] + H+[side 2] = propanoyl-CoA + CO2 + Na+[side 2]
Other name(s): methylmalonyl-coenzyme A decarboxylase (ambiguous); (S)-2-methyl-3-oxopropanoyl-CoA carboxy-lyase (incorrect); (S)-methylmalonyl-CoA carboxy-lyase (ambiguous)
Systematic name: (S)-methylmalonyl-CoA carboxy-lyase (propanoyl-CoA-forming, sodium-transporting)
Comments: This bacterial enzyme couples the decarboxylation of (S)-methylmalonyl-CoA to propanoyl-CoA to the vectorial transport of Na+ across the cytoplasmic membrane, thereby creating a sodium ion motive force that is used for ATP synthesis. It is a membrane-associated biotin protein and is strictly dependent on sodium ions for activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37289-44-4
1.  Galivan, J.H. and Allen, S.H.G. Methylmalonyl coenzyme A decarboxylase. Its role in succinate decarboxylation by Micrococcus lactilyticus. J. Biol. Chem. 243 (1968) 1253–1261. [PMID: 5646172]
2.  Hilpert, W. and Dimroth, P. Conversion of the chemical energy of methylmalonyl-CoA decarboxylation into a Na+ gradient. Nature 296 (1982) 584–585. [PMID: 7070502]
3.  Hoffmann, A., Hilpert, W. and Dimroth, P. The carboxyltransferase activity of the sodium-ion-translocating methylmalonyl-CoA decarboxylase of Veillonella alcalescens. Eur. J. Biochem. 179 (1989) 645–650. [DOI] [PMID: 2920730]
4.  Huder, J.B. and Dimroth, P. Expression of the sodium ion pump methylmalonyl-coenzyme A-decarboxylase from Veillonella parvula and of mutated enzyme specimens in Escherichia coli. J. Bacteriol. 177 (1995) 3623–3630. [PMID: 7601825]
5.  Bott, M., Pfister, K., Burda, P., Kalbermatter, O., Woehlke, G. and Dimroth, P. Methylmalonyl-CoA decarboxylase from Propionigenium modestum--cloning and sequencing of the structural genes and purification of the enzyme complex. Eur. J. Biochem. 250 (1997) 590–599. [PMID: 9428714]
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